Proteoglycans will be purified from small, medium, large, and cystic bovine ovarian follicles using Sepharose CL-2B and DEAE-ion exchange chromatography. Associative and dissociative conditions will be compared. Changes in the covalently attached glycosaminoglycans will be quantitated using high performance liquid chromatography. Granulosa cells from small and large follicles will be cultured with radioactive precursors for protein and carbohydrate biosynthesis. The effects of various polypeptide hormones on stimulation of secreted radiolabelled glycosaminoglycans will be evaluated. Antibodies raised against purified proteoglycan will be used to precipitate radiolabelled proteoglycan. Enzymatic and acidic hydrolysis products of radiolabelled and native proteoglycan and glycosaminoglycan will be compared using reverse-phase liquid chromatography. If FSH continues to be the most potent hormone in terms of stimulating proteoglycan biosynthesis, a bioassay will be statistically validated. Finally, bovine cumulus-oocyte complexes will be cultured with gonadotropins, gonadal steroids, and inhibitors of steroidal biosynthesis. Hormonal control of mucification with accompanying morphological changes will be examined by correlating cumulus expansion with incorporation of tritiated glucosamine into glycosaminoglycans.